Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes
Several polypeptides of about 120, 96, 85, 60 and 38 kDa are shown to be radiolabeled during incubation of the mono- and polyribosome fraction of rabbit reticulocytes with [ 32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacr...
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Veröffentlicht in: | FEBS letters 1984-10, Vol.176 (1), p.261-263 |
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creator | Sitikov, A.S. Davydova, E.K. Ovchinnikov, L.P. |
description | Several polypeptides of about 120, 96, 85, 60 and 38 kDa are shown to be radiolabeled during incubation of the mono- and polyribosome fraction of rabbit reticulocytes with [
32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacrylamide gel. The addition of pure EF-2 to the polyribosome fraction results in an increase of the radioactive label in this polypeptide band. From this it is concluded that both endogenous and added EF-2 is ADP-ribosylated by an enzyme associated with polyribosomes. A possibility of regulation of protein synthesis through endogenous ADP-ribosylation in vivo is considered. |
doi_str_mv | 10.1016/0014-5793(84)80953-9 |
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32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacrylamide gel. The addition of pure EF-2 to the polyribosome fraction results in an increase of the radioactive label in this polypeptide band. From this it is concluded that both endogenous and added EF-2 is ADP-ribosylated by an enzyme associated with polyribosomes. A possibility of regulation of protein synthesis through endogenous ADP-ribosylation in vivo is considered.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(84)80953-9</identifier><identifier>PMID: 6092136</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adenosine Diphosphate Ribose - metabolism ; ADP-ribosylation ; Animals ; Biological and medical sciences ; Elongation factor 2 ; Fundamental and applied biological sciences. Psychology ; Molecular and cellular biology ; Molecular genetics ; NAD - metabolism ; Nucleoside Diphosphate Sugars - metabolism ; Nucleotidyltransferases - metabolism ; Peptide Elongation Factor 2 ; Peptide Elongation Factors - metabolism ; Poly(ADP-ribose) Polymerases ; Polyribosome ; Polyribosomes - metabolism ; Protein biosynthesis regulation ; Rabbit reticulocyte ; Rabbits ; Reticulocytes - metabolism ; Translation. Translation factors. Protein processing</subject><ispartof>FEBS letters, 1984-10, Vol.176 (1), p.261-263</ispartof><rights>1984</rights><rights>FEBS Letters 176 (1984) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4419-35da5c76d723bfcf0f891d03b0b4279a2c171dd1e22b650822f3dfa90258a1de3</citedby><cites>FETCH-LOGICAL-c4419-35da5c76d723bfcf0f891d03b0b4279a2c171dd1e22b650822f3dfa90258a1de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(84)80953-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9149826$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6092136$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sitikov, A.S.</creatorcontrib><creatorcontrib>Davydova, E.K.</creatorcontrib><creatorcontrib>Ovchinnikov, L.P.</creatorcontrib><title>Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Several polypeptides of about 120, 96, 85, 60 and 38 kDa are shown to be radiolabeled during incubation of the mono- and polyribosome fraction of rabbit reticulocytes with [
32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacrylamide gel. The addition of pure EF-2 to the polyribosome fraction results in an increase of the radioactive label in this polypeptide band. From this it is concluded that both endogenous and added EF-2 is ADP-ribosylated by an enzyme associated with polyribosomes. A possibility of regulation of protein synthesis through endogenous ADP-ribosylation in vivo is considered.</description><subject>Adenosine Diphosphate Ribose - metabolism</subject><subject>ADP-ribosylation</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Elongation factor 2</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>NAD - metabolism</subject><subject>Nucleoside Diphosphate Sugars - metabolism</subject><subject>Nucleotidyltransferases - metabolism</subject><subject>Peptide Elongation Factor 2</subject><subject>Peptide Elongation Factors - metabolism</subject><subject>Poly(ADP-ribose) Polymerases</subject><subject>Polyribosome</subject><subject>Polyribosomes - metabolism</subject><subject>Protein biosynthesis regulation</subject><subject>Rabbit reticulocyte</subject><subject>Rabbits</subject><subject>Reticulocytes - metabolism</subject><subject>Translation. Translation factors. Protein processing</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhi0EKtvCG4CUA0LlEPDYTmJfKpWyC0iV4ABny7HHlVE2XuwsKG9Pson2CJysmf-bGc8_hLwA-hYo1O8oBVFWjeLXUryRVFW8VI_IBmTDSy5q-ZhszshTcpnzDzrFEtQFuaipYsDrDbHb3sUH7OMxF7cfvpYptDGPnRlC7IvoC-xi_7BE3tghpoIVoS8OsRtPaNxj4dOkrHwybRuGIuEQ7LGLdhwwPyNPvOkyPl_fK_J9t_1296m8__Lx893tfWmFAFXyypnKNrVrGG-99dRLBY7ylraCNcowCw04B8hYW1dUMua580ZRVkkDDvkVeb30PaT484h50PuQLXad6XHaT0tgiktJ_wmCoAKEhAkUC2hTzDmh14cU9iaNGqiej6Bnh_XssJZCn46g1VT2cu1_bPfozkWr65P-atVNtqab_OttyGdMgVCSzdhuwX6HDsf_Gq132_dsFua8FKfs_J-bpRFO7v8KmHS2AXuLLiS0g3Yx_H2hPzSlts0</recordid><startdate>19841015</startdate><enddate>19841015</enddate><creator>Sitikov, A.S.</creator><creator>Davydova, E.K.</creator><creator>Ovchinnikov, L.P.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19841015</creationdate><title>Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes</title><author>Sitikov, A.S. ; Davydova, E.K. ; Ovchinnikov, L.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4419-35da5c76d723bfcf0f891d03b0b4279a2c171dd1e22b650822f3dfa90258a1de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Adenosine Diphosphate Ribose - metabolism</topic><topic>ADP-ribosylation</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Elongation factor 2</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>NAD - metabolism</topic><topic>Nucleoside Diphosphate Sugars - metabolism</topic><topic>Nucleotidyltransferases - metabolism</topic><topic>Peptide Elongation Factor 2</topic><topic>Peptide Elongation Factors - metabolism</topic><topic>Poly(ADP-ribose) Polymerases</topic><topic>Polyribosome</topic><topic>Polyribosomes - metabolism</topic><topic>Protein biosynthesis regulation</topic><topic>Rabbit reticulocyte</topic><topic>Rabbits</topic><topic>Reticulocytes - metabolism</topic><topic>Translation. Translation factors. Protein processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sitikov, A.S.</creatorcontrib><creatorcontrib>Davydova, E.K.</creatorcontrib><creatorcontrib>Ovchinnikov, L.P.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sitikov, A.S.</au><au>Davydova, E.K.</au><au>Ovchinnikov, L.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1984-10-15</date><risdate>1984</risdate><volume>176</volume><issue>1</issue><spage>261</spage><epage>263</epage><pages>261-263</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Several polypeptides of about 120, 96, 85, 60 and 38 kDa are shown to be radiolabeled during incubation of the mono- and polyribosome fraction of rabbit reticulocytes with [
32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacrylamide gel. The addition of pure EF-2 to the polyribosome fraction results in an increase of the radioactive label in this polypeptide band. From this it is concluded that both endogenous and added EF-2 is ADP-ribosylated by an enzyme associated with polyribosomes. A possibility of regulation of protein synthesis through endogenous ADP-ribosylation in vivo is considered.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>6092136</pmid><doi>10.1016/0014-5793(84)80953-9</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Diphosphate Ribose - metabolism ADP-ribosylation Animals Biological and medical sciences Elongation factor 2 Fundamental and applied biological sciences. Psychology Molecular and cellular biology Molecular genetics NAD - metabolism Nucleoside Diphosphate Sugars - metabolism Nucleotidyltransferases - metabolism Peptide Elongation Factor 2 Peptide Elongation Factors - metabolism Poly(ADP-ribose) Polymerases Polyribosome Polyribosomes - metabolism Protein biosynthesis regulation Rabbit reticulocyte Rabbits Reticulocytes - metabolism Translation. Translation factors. Protein processing |
title | Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes |
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